ID M2PFC9_CERS8 Unreviewed; 1444 AA.
AC M2PFC9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Protein transport protein SEC31 {ECO:0000256|ARBA:ARBA00021236};
DE AltName: Full=Protein transport protein sec31 {ECO:0000256|ARBA:ARBA00013507};
GN ORFNames=CERSUDRAFT_116810 {ECO:0000313|EMBL:EMD34634.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD34634.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD34634.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD34634.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
CC -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules. {ECO:0000256|ARBA:ARBA00025471}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004299}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the WD repeat SEC31 family.
CC {ECO:0000256|ARBA:ARBA00009358}.
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DR EMBL; KB445802; EMD34634.1; -; Genomic_DNA.
DR STRING; 914234.M2PFC9; -.
DR HOGENOM; CLU_003033_2_0_1; -.
DR OrthoDB; 149677at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR Gene3D; 1.25.40.1030; -; 1.
DR Gene3D; 1.20.940.10; Functional domain of the splicing factor Prp18; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR040251; SEC31-like.
DR InterPro; IPR009917; SRA1/Sec31.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR13923; SEC31-RELATED PROTEIN; 1.
DR PANTHER; PTHR13923:SF11; SECRETORY 31, ISOFORM D; 1.
DR Pfam; PF07304; SRA1; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022892};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 123..165
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 281..323
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1308..1442
FT /note="SRA1/Sec31"
FT /evidence="ECO:0000259|Pfam:PF07304"
FT REGION 518..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1057
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1335
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1444 AA; 153630 MW; CDAC70B78E23EBC0 CRC64;
MKLKEIHRTS TFAWSPSPSL PLLATGTVAG ALDESFSNNG QLEIWAPDFL DKNEYDLGGE
DQAGPNATIT TSSRFNRLAW GYTDGGRERG VLVAGMENGE LDIWDPSKIL ANADPAESLI
LRNKSHTGPI RGLDFNPIQT NLFSSGAVNG EIYIWDLKDP SKPYSPGTRS TKLDEITALA
WNHHVQYALA ASSSTGYTVV WDLRGKREVA ALAYGGGAGT LAGGMQGYGA AGMHVGGRRG
MSDVAWHPDN ATRLVTSSED DTSPIIMVWD LRNARAPEKI LTGHEKGVLS LSWCKQDPDL
LLSCGKDNRA LCWNPQTSEI IGELPSADNW AFQVQWCPRN PDLFATAFFD GTIGIHSIQS
TNESADAPLA TQPDASDIFG APGFSRASQA TLSLKHPPKW LRRPSSSSFG YGGKLVTVSN
LPSTQGKNQS SVVHIRKVAT EGDIADRASK LRTAIEDEKL DEFAQEKSAE ATDGTASWKA
LSSLFKANSR DELITLLGFS KEEIATRVAE AVAKLKASAD STIEEDVTEV DGETRESVVS
FAEPEREAED KAEAEDTDAS GVAEATPSEV SAGAASDATG TTHLADNEST TTAPSLFGDD
AIGTPQTDAA ADFFGSIGTG RTSEDDQMQI PHHNYALDSS VAATIGSGPS SVASEALKNN
TFRIYPADES ETDRLVTKAL VLGDFESAVS LCLSTSRFAD AILLAVKGGP ELLRRTQKAY
FEKRTTALPY LRLFQSIVTN DLADIVQNAD LQEWQEIFVV LCTYASQEEF SSLTEQLGQR
LEFQSSLIKT SGAADAEQRA AEFRRNATLT YLAAGRLERL VNIWIEELSE QEKSLIADAD
NLSGSRYTAH ALALQNFIEK VTVFRNAIHY NDLDMAQKSS AAEAETKLYK LTTLYDRYFE
YADLLAAQGL VREALVFLKL TPADYTGSEG TPLDFSEIRE RILRASGEVA APARTVSLPV
STSAIPAQPL SMAASTSAYP YSQYAAPSQP TVSHVHAPSV YESYNAPAVA QAPNPYGPAA
PAAHPQQHYQ PTAPMSYGAP GPYAPAPTQP AMAPPAPVMA PRGANATPSA PPLAPPPQGL
PKRENGGWND APALAAQRRT PANANAHRPA AITSPFPHAP SPGPLPTSPY NQGPPATLPP
PPRPGSVQAR PPPPPGQRMP PPQQGPGQYP PHARPPSGPP VPPSQHMPPP PPPGRAMAPP
QAQMARPGPP PTGPYGSGGP VPGQGSHGHM QPPAPGVNPV PQGPPGPYAH APPAAGFGRG
TPPPGPPPPG PGGAPYGRPP QNAQFAPPPQ GAPRAGPPAN TLQGPPRGGT PGSAAPPQAA
PPRANPGPPQ PKYPPGDRSH IAEEMRPVYT VISGQLERLK QTTPPQQKRL VDDLERRINP
LFDALNCETL SKPVCEQLIV LARAMDQHDR DVAMAIHMDL LTRGSLTDDI GLWMSGIKQL
IMRL
//
